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Database: UniProt
Entry: P9WMQ2
LinkDB: P9WMQ2
Original site: P9WMQ2 
ID   RECB_MYCTO              Reviewed;        1094 AA.
AC   P9WMQ2; L0T4F0; P96920;
DT   16-APR-2014, integrated into UniProtKB/Swiss-Prot.
DT   16-APR-2014, sequence version 1.
DT   05-DEC-2018, entry version 34.
DE   RecName: Full=RecBCD enzyme subunit RecB {ECO:0000255|HAMAP-Rule:MF_01485};
DE            EC=3.1.11.5 {ECO:0000255|HAMAP-Rule:MF_01485};
DE   AltName: Full=Exonuclease V subunit RecB {ECO:0000255|HAMAP-Rule:MF_01485};
DE            Short=ExoV subunit RecB {ECO:0000255|HAMAP-Rule:MF_01485};
DE   AltName: Full=Helicase/nuclease RecBCD subunit RecB {ECO:0000255|HAMAP-Rule:MF_01485};
GN   Name=recB {ECO:0000255|HAMAP-Rule:MF_01485}; OrderedLocusNames=MT0658;
OS   Mycobacterium tuberculosis (strain CDC 1551 / Oshkosh).
OC   Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC   Mycobacterium; Mycobacterium tuberculosis complex.
OX   NCBI_TaxID=83331;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CDC 1551 / Oshkosh;
RX   PubMed=12218036; DOI=10.1128/JB.184.19.5479-5490.2002;
RA   Fleischmann R.D., Alland D., Eisen J.A., Carpenter L., White O.,
RA   Peterson J.D., DeBoy R.T., Dodson R.J., Gwinn M.L., Haft D.H.,
RA   Hickey E.K., Kolonay J.F., Nelson W.C., Umayam L.A., Ermolaeva M.D.,
RA   Salzberg S.L., Delcher A., Utterback T.R., Weidman J.F., Khouri H.M.,
RA   Gill J., Mikula A., Bishai W., Jacobs W.R. Jr., Venter J.C.,
RA   Fraser C.M.;
RT   "Whole-genome comparison of Mycobacterium tuberculosis clinical and
RT   laboratory strains.";
RL   J. Bacteriol. 184:5479-5490(2002).
CC   -!- FUNCTION: A helicase/nuclease that prepares dsDNA breaks (DSB) for
CC       recombinational DNA repair. Binds to DSBs and unwinds DNA via a
CC       highly rapid and processive ATP-dependent bidirectional helicase
CC       activity. Unwinds dsDNA until it encounters a Chi (crossover
CC       hotspot instigator) sequence from the 3' direction. Cuts ssDNA a
CC       few nucleotides 3' to the Chi site. The properties and activities
CC       of the enzyme are changed at Chi. The Chi-altered holoenzyme
CC       produces a long 3'-ssDNA overhang and facilitates RecA-binding to
CC       the ssDNA for homologous DNA recombination and repair. Holoenzyme
CC       degrades any linearized DNA that is unable to undergo homologous
CC       recombination. In the holoenzyme this subunit contributes ATPase,
CC       3'-5' helicase, exonuclease activity and loads RecA onto ssDNA.
CC       {ECO:0000255|HAMAP-Rule:MF_01485}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=Exonucleolytic cleavage (in the presence of ATP) in
CC         either 5'- to 3'- or 3'- to 5'-direction to yield 5'-
CC         phosphooligonucleotides.; EC=3.1.11.5;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_01485};
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_01485};
CC   -!- SUBUNIT: Heterotrimer of RecB, RecC and RecD. All subunits
CC       contribute to DNA-binding. Interacts with RecA.
CC       {ECO:0000255|HAMAP-Rule:MF_01485}.
CC   -!- DOMAIN: The N-terminal DNA-binding domain is a ssDNA-dependent
CC       ATPase and has ATP-dependent 3'-5' helicase function. This domain
CC       interacts with RecC. {ECO:0000255|HAMAP-Rule:MF_01485}.
CC   -!- DOMAIN: The C-terminal domain has nuclease activity and interacts
CC       with RecD. It interacts with RecA, facilitating its loading onto
CC       ssDNA. {ECO:0000255|HAMAP-Rule:MF_01485}.
CC   -!- SIMILARITY: Belongs to the helicase family. UvrD subfamily.
CC       {ECO:0000255|HAMAP-Rule:MF_01485}.
DR   EMBL; AE000516; AAK44882.1; -; Genomic_DNA.
DR   PIR; C70612; C70612.
DR   RefSeq; WP_003905355.1; NZ_KK341227.1.
DR   ProteinModelPortal; P9WMQ2; -.
DR   PRIDE; P9WMQ2; -.
DR   EnsemblBacteria; AAK44882; AAK44882; MT0658.
DR   KEGG; mtc:MT0658; -.
DR   PATRIC; fig|83331.31.peg.698; -.
DR   KO; K03582; -.
DR   OrthoDB; POG091H02P3; -.
DR   Proteomes; UP000001020; Chromosome.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0004003; F:ATP-dependent DNA helicase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0003677; F:DNA binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0008854; F:exodeoxyribonuclease V activity; IEA:UniProtKB-EC.
DR   GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0000724; P:double-strand break repair via homologous recombination; IEA:UniProtKB-UniRule.
DR   Gene3D; 3.90.320.10; -; 1.
DR   HAMAP; MF_01485; RecB; 1.
DR   InterPro; IPR014017; DNA_helicase_UvrD-like_C.
DR   InterPro; IPR000212; DNA_helicase_UvrD/REP.
DR   InterPro; IPR011604; Exonuc_phg/RecB_C.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR038726; PDDEXK_AddAB-type.
DR   InterPro; IPR004586; RecB.
DR   InterPro; IPR011335; Restrct_endonuc-II-like.
DR   InterPro; IPR014016; UvrD-like_ATP-bd.
DR   InterPro; IPR034739; UvrD/AddA_N.
DR   PANTHER; PTHR11070; PTHR11070; 2.
DR   PANTHER; PTHR11070:SF23; PTHR11070:SF23; 2.
DR   Pfam; PF12705; PDDEXK_1; 1.
DR   Pfam; PF00580; UvrD-helicase; 1.
DR   Pfam; PF13361; UvrD_C; 1.
DR   SUPFAM; SSF52540; SSF52540; 1.
DR   SUPFAM; SSF52980; SSF52980; 1.
DR   TIGRFAMs; TIGR00609; recB; 1.
DR   PROSITE; PS51198; UVRD_HELICASE_ATP_BIND; 1.
DR   PROSITE; PS51217; UVRD_HELICASE_CTER; 1.
PE   3: Inferred from homology;
KW   ATP-binding; Complete proteome; DNA damage; DNA repair; DNA-binding;
KW   Exonuclease; Helicase; Hydrolase; Magnesium; Metal-binding; Nuclease;
KW   Nucleotide-binding.
FT   CHAIN         1   1094       RecBCD enzyme subunit RecB.
FT                                /FTId=PRO_0000427264.
FT   DOMAIN        1    326       UvrD-like helicase ATP-binding.
FT                                {ECO:0000255|HAMAP-Rule:MF_01485}.
FT   DOMAIN      357    613       UvrD-like helicase C-terminal.
FT                                {ECO:0000255|HAMAP-Rule:MF_01485}.
FT   NP_BIND      21     28       ATP. {ECO:0000255|HAMAP-Rule:MF_01485}.
FT   REGION        1    764       DNA-binding and helicase activity,
FT                                interacts with RecC. {ECO:0000255|HAMAP-
FT                                Rule:MF_01485}.
FT   REGION      775   1094       Nuclease activity, interacts with RecD
FT                                and RecA. {ECO:0000255|HAMAP-
FT                                Rule:MF_01485}.
FT   ACT_SITE    989    989       For nuclease activity.
FT                                {ECO:0000255|HAMAP-Rule:MF_01485}.
FT   METAL       838    838       Magnesium; via tele nitrogen.
FT                                {ECO:0000255|HAMAP-Rule:MF_01485}.
FT   METAL       975    975       Magnesium. {ECO:0000255|HAMAP-
FT                                Rule:MF_01485}.
FT   METAL       989    989       Magnesium. {ECO:0000255|HAMAP-
FT                                Rule:MF_01485}.
SQ   SEQUENCE   1094 AA;  118722 MW;  31262D376875C201 CRC64;
     MDRFELLGPL PREGTTTVLE ASAGTGKTFA LAGLVTRYLA ETAATLDEML LITFNRAASR
     ELRERVRGQI VEAVGALQGD APPSGELVEH LLRGSDAERA QKRSRLRDAL ANFDAATIAT
     THEFCGSVLK SLGVAGDNAA DVELKESLTD LVTEIVDDRY LANFGRQETD PELTYAEALA
     LALAVVDDPC AQLRPPDPEP GSKAAVRLRF AAEVLEELER RKGRLRAQGF NDLLIRLATA
     LEAADSPARD RMRERWRIVL VDEFQDTDPM QWRVLERAFS RHSALILIGD PKQAIYGFRG
     GDIHTYLKAA GTADARYTLG VNWRSDRALV ESLQTVLRDA TLGHADIVVR GTDAHHAGHR
     LASAPRPAPF RLRVVKRHTL GYDGTAHVPI EALRRHIPDD LAADVAALLA SGATFAGRPV
     VAADIAVIVE HHKDARACRN ALAEAGIPAI YTGDTDVFAS QAAKDWLCLL EAFDAPQRSG
     LVRAAACTMF FGETAESLAA EGDALTDRVA GTLREWADHA RHRGVAAVFQ AAQLAGMGRR
     VLSQRGGERD LTDLAHIAQL LHEAAHRERL GLPGLRDWLR RQAKAGAGPP EHNRRLDSDA
     AAVQIMTVFV AKGLQFPIVY LPFAFNRNVR SDDILLYHDD GTRCLYIGGK DGGAQRRTVE
     GLNRVEAAHD NLRLTYVALT RAQSQVVAWW APTFDEVNGG LSRLLRGRRP GQSQVPDRCT
     PRVTDEQAWA VFAQWEAAGG PSVEESVIGA RSSLEKPVPV PGFEVRHFHR RIDTTWRRTS
     YSDLVRGSEA VTVTSEPAAG GRADEVEIAV VAAPGSGADL TSPLAALPSG ASFGSLVHAV
     LETADPAAPD LAAELEAQVR RHAPWWTVDV DHAQLAPELA RALLPMHDTP LGPAAAALTL
     RQIGVRDRLR ELDFEMPLAG GDLRGRSPDV SLADVGELLA SHLPGDDPLS PYADRLGSAG
     LGDQPLRGYL AGSIDVVLRL PGQRYLVVDY KTNHLGDTAA DYGFERLTEA MLHSDYPLQA
     LLYVVVLHRF LRWRQRDYAP ARHLGGVLYL FVRGMCGAAT PVTAGHPAGV FTWNPPTALV
     VALSDLLDRG RLQS
//
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